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Difference between revisions of "Glycoside Hydrolase Family 64"
| Line 34: | Line 34: | ||
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
| − | GH64 enzymes follow an [[inverting]] mechanism, | + | GH64 enzymes follow an [[inverting]] mechanism, first shown by 1H-NMR during the hydrolysis of laminarin <cite>Nishimura2001</cite>. |
== Catalytic Residues == | == Catalytic Residues == | ||
Revision as of 09:42, 6 May 2020
This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.
- Author: ^^^Julie Grondin^^^
- Responsible Curator: ^^^Harry Brumer^^^
| Glycoside Hydrolase Family GH64 | |
| Clan | GH-x |
| Mechanism | inverting |
| Active site residues | known |
| CAZy DB link | |
| https://www.cazy.org/GH64.html | |
Substrate specificities
All characterized members of the GH64 family are laminaripentaose-producing β-1,3-glucanases (EC 3.2.1.39] from the GH64-TLP (thaumatin-like protein) superfamily. They are found in bacteria and fungal species, and are particularly abundant in the genomes of various Streptomyces and Fusarium species.
Activity has been shown on insoluble and soluble β-1,3-glucans, including curdlan [1, 2, 3], colloidal pachyman [1, 3, 4], laminarin [1, 3, 4], and zymosan A [1, 2], a commercial preparation of partially-purified yeast cell walls (contains branched glucans).
Kinetics and Mechanism
GH64 enzymes follow an inverting mechanism, first shown by 1H-NMR during the hydrolysis of laminarin [4].
Catalytic Residues
Content is to be added here.
Three-dimensional structures
Content is to be added here.
Family Firsts
- First stereochemistry determination
- Laminaripentaose-producing β-1,3-glucanase (LPHase) from Streptomyces matensis DIC-108.[4]
- First catalytic nucleophile identification
- Laminaripentaose-producing β-1,3-glucanase (LPHase) from Streptomyces matensis DIC-108.[3]
- First general acid/base residue identification
- Laminaripentaose-producing β-1,3-glucanase (LPHase) from Streptomyces matensis DIC-108.[3]
- First 3-D structure
- Laminaripentaose-producing β-1,3-glucanase (LPHase) from Streptomyces matensis DIC-108.[3]
References
-
Nakabayashi, M. (1998) Structure of the gene encoding laminaripentaose-producing β-1,3-glucanase (LPHase) of Streptomyces matensis DIC-108. J. Ferment. Bioengineer. 85, 459-464. DOI=10.1016/s0922-338x(98)80062-7
- Palumbo JD, Sullivan RF, and Kobayashi DY. (2003). Molecular characterization and expression in Escherichia coli of three beta-1,3-glucanase genes from Lysobacter enzymogenes strain N4-7. J Bacteriol. 2003;185(15):4362-70. DOI:10.1128/JB.185.15.4362-4370.2003 |
- Wu HM, Liu SW, Hsu MT, Hung CL, Lai CC, Cheng WC, Wang HJ, Li YK, and Wang WC. (2009). Structure, mechanistic action, and essential residues of a GH-64 enzyme, laminaripentaose-producing beta-1,3-glucanase. J Biol Chem. 2009;284(39):26708-15. DOI:10.1074/jbc.M109.010983 |
- Nishimura T, Bignon C, Allouch J, Czjzek M, Darbon H, Watanabe T, and Henrissat B. (2001). Streptomyces matensis laminaripentaose hydrolase is an 'inverting' beta-1,3-glucanase. FEBS Lett. 2001;499(1-2):187-90. DOI:10.1016/s0014-5793(01)02551-0 |